Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein

Autor: Edgar D. Páez-Pérez, Miriam Livier Llamas-García, Claudia G. Benítez-Cardoza, Gabriela M. Montero-Morán, Samuel Lara-González

Publikováno v: ACS Omega, Vol 5, Iss 40, Pp 25841-25847 (2020)

Externí odkaz: https://doaj.org/article/959f7c3b12954f5dba7930a693f95e20

Self-Association of Enolase from Trichomonas vaginalis. Monomers, Dimers, and Octamers Coexist in Solution

Autor: Enrique Lima, Luis G. Brieba, Samuel Lara-González, Claudia G. Benítez-Cardoza, Victor Lara, Elibeth Mirasol-Meléndez

Publikováno v: ACS Omega. 3:17871-17880

We used small-angle X-ray scattering to study the self-association of enolase from Trichomonas vaginalis as a function of the protein concentration and cosolute type. We observed coexisting monomer...

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d00a054cc5d7b03269b79c3098950f36
https://doi.org/10.1021/acsomega.8b02197

The RNA Polymerase ? Subunit Recognizes the DNA Shape of the Upstream Promoter Element

Autor: Catherine L. Lawson, Jens J. Birktoft, Andrew A. Napoli, Ana Carolina Dantas Machado, Satyanarayan Rao, Samuel Lara-González, Rosa Di Felice, Remo Rohs

Publikováno v: Biochemistry (Easton) 59 (2020): 4523–4532. doi:10.1021/acs.biochem.0c00571
info:cnr-pdr/source/autori:Lara-Gonzalez S.; Dantas MacHado A.C.; Rao S.; Napoli A.A.; Birktoft J.; Di Felice R.; Rohs R.; Lawson C.L./titolo:The RNA Polymerase ? Subunit Recognizes the DNA Shape of the Upstream Promoter Element/doi:10.1021%2Facs.biochem.0c00571/rivista:Biochemistry (Easton)/anno:2020/pagina_da:4523/pagina_a:4532/intervallo_pagine:4523–4532/volume:59
Biochemistry

We demonstrate here that the α subunit C-terminal domain of Escherichia coli RNA polymerase (αCTD) recognizes the upstream promoter (UP) DNA element via its characteristic minor groove shape and electrostatic potential. In two compositionally disti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::619867040dae39b8e02347d2c139a0e3
https://publications.cnr.it/doc/442846

Human Gpn1 purified from bacteria binds guanine nucleotides and hydrolyzes GTP as a protein dimer stabilized by its C-terminal tail

Autor: Samuel Lara-González, Gabriela M. Montero-Morán, Gema R. Cristóbal-Mondragón, Andrés Hernández-Arana, Sonia G. Peña-Gómez, José A. Guerra-Moreno, Daniel A. Fernández-Velasco, Violeta Romero, Mónica R. Calera, Rogelio González-González, Roberto Sánchez-Olea

Publikováno v: Protein Expression and Purification. 132:85-96

The essential GTPase Gpn1 mediates RNA polymerase II nuclear targeting and controls microtubule dynamics in yeast and human cells by molecular mechanisms still under investigation. Here, we purified human HisGpn1 expressed as a recombinant protein in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88eca1fd25b91bd40589bbcb9e5f4146
https://doi.org/10.1016/j.pep.2017.01.009

Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana

Autor: Carlos H. Trasviña-Arenas, Pedro Jimenez-Sandoval, Noe Baruch-Torres, Luis G. Brieba, Robert Winkler, Corina Diaz-Quezada, Laura Margarita López-Castillo, Samuel Lara-González

Publikováno v: Frontiers in Plant Science, Vol 7 (2016)

In plants triosephosphate isomerase (TPI) interconverts glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP) during glycolysis, gluconeogenesis, and the Calvin-Benson cycle. The nuclear genome of land plants encodes two tpi genes, o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d886442df363aa762dea35d0f358c59
https://doi.org/10.3389/fpls.2016.01817